6M1C
Crystal structure of RsmD methyltransferase of M. tuberculosis in complex with sinefungin reveals key interactions
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE MASSIF-3 |
Synchrotron site | ESRF |
Beamline | MASSIF-3 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2018-02-10 |
Detector | DECTRIS EIGER2 X 4M |
Wavelength(s) | 0.887821 |
Spacegroup name | P 32 2 1 |
Unit cell lengths | 55.191, 55.191, 99.641 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 47.800 - 2.401 |
R-factor | 0.2052 |
Rwork | 0.203 |
R-free | 0.23610 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3p9n |
RMSD bond length | 0.007 |
RMSD bond angle | 0.838 |
Data reduction software | XDS |
Data scaling software | Aimless |
Phasing software | PHASER |
Refinement software | PHENIX ((1.14_3260: ???)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 47.800 | 2.490 |
High resolution limit [Å] | 2.400 | 2.400 |
Number of reflections | 7293 | 745 |
<I/σ(I)> | 12 | |
Completeness [%] | 100.0 | |
Redundancy | 9.2 | |
CC(1/2) | 0.999 | 0.939 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.4 | 297 | 0.1 MTris-HCl, 3.2 M Potassium acetate |